. Author manuscript; available in PMC: 2010 Oct 2.

Published in final edited form as: J Mol Biol. 2009 Aug 6;392(4):1102–1115. doi: 10.1016/j.jmb.2009.07.093

Table 1.

Statistical summary of the RAMD simulations of the carazolol-bound crystal structure. The results are separately listed from 60 simulations with 4 different accelerations and 40 simulations with the smallest acceleration. The latter results are in the gray-shaded rows.

Pathway	Egress point	Number of trajectories	Acceleration (kcal/Å·g)	Trajectory length (ps)
A	Extracellular opening	41 (19^a, 21^b)	0.20, 0.23, 0.25, 0.30	22–976
A	Extracellular opening	28 (11^a, 17 ^b)	0.20	22–928
B	H4–H5 cleft	16	0.20, 0.23, 0.25, 0.30	16–878
B	H4–H5 cleft	5	0.20	144–596
C	H5–H6 cleft	2	0.30, 0.30	90, 104
C	H5–H6 cleft	1	0.20	152
D	H1–H2 cleft	1	0.20	500
D	H1–H2 cleft	1	0.20	930
E	H1–H7 cleft	0
E	H1–H7 cleft	2	0.20	564,1000
F	H6–H7 cleft	0
F	H6–H7 cleft	1	0.20	438
	No egress	0
	No egress	2	0.20	1000

^a,b

carazolol passed out of the receptor from the “left” side (sub-pathway A1) and the “right” side(sub-pathway A2) of the D192-K305 salt bridge, respectively.